ID Q9TLR1_CYACA Unreviewed; 61 AA.
AC Q9TLR1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Photosystem II reaction center protein Z {ECO:0000256|ARBA:ARBA00021665, ECO:0000256|RuleBase:RU003472};
GN Name=ycf9 {ECO:0000313|EMBL:AAF12886.1};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAF12886.1}.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771 {ECO:0000313|EMBL:AAF12886.1};
RN [1] {ECO:0000313|EMBL:AAF12886.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RK1 {ECO:0000313|EMBL:AAF12886.1};
RA Gloeckner G., Rosenthal A., Valentin K.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAF12886.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RK1 {ECO:0000313|EMBL:AAF12886.1};
RX PubMed=11040290;
RA Glockner G., Rosenthal A., Valentin K.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
CC -!- FUNCTION: Controls the interaction of photosystem II (PSII) cores with
CC the light-harvesting antenna, regulates electron flow through the 2
CC photosystem reaction centers. PSII is a light-driven water
CC plastoquinone oxidoreductase, using light energy to abstract electrons
CC from H(2)O, generating a proton gradient subsequently used for ATP
CC formation. {ECO:0000256|RuleBase:RU003472}.
CC -!- SUBUNIT: PSII is composed of 1 copy each of membrane proteins PsbA,
CC PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT,
CC PsbY, PsbZ, Psb30/Ycf12, at least 3 peripheral proteins of the oxygen-
CC evolving complex and a large number of cofactors. It forms dimeric
CC complexes. {ECO:0000256|ARBA:ARBA00038734}.
CC -!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000256|ARBA:ARBA00008367,
CC ECO:0000256|RuleBase:RU003472}.
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DR EMBL; AF022186; AAF12886.1; -; Genomic_DNA.
DR RefSeq; NP_045208.1; NC_001840.1.
DR AlphaFoldDB; Q9TLR1; -.
DR GeneID; 800123; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR Gene3D; 1.10.287.740; Photosystem II PsbZ, reaction centre; 1.
DR InterPro; IPR002644; PSII_PsbZ.
DR InterPro; IPR036512; PSII_PsbZ_sf.
DR Pfam; PF01737; Ycf9; 1.
DR SUPFAM; SSF161055; PsbZ-like; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AAF12886.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU003472};
KW Photosystem II {ECO:0000256|ARBA:ARBA00023276,
KW ECO:0000256|RuleBase:RU003472}; Plastid {ECO:0000313|EMBL:AAF12886.1};
KW Reaction center {ECO:0000256|ARBA:ARBA00022469,
KW ECO:0000256|RuleBase:RU003472};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU003472};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003472};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 61 AA; 6911 MW; C4C44154EEAFF83E CRC64;
MSILLQFFII SIIFFSLILV ILVPSQLSLQ SGWQVSKSRF IALFTIWASM ILISGFISVF
V
//